TY - JOUR
T1 - Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus
AU - Pendini, Nicole Renee
AU - Polyak, Steven W
AU - Booker, Grant William
AU - Wallace, John Campbell
AU - Wilce, Matthew Charles James
PY - 2008
Y1 - 2008
N2 - Biotin protein ligase from Staphylococcus aureus catalyses the biotinylation of acetyl-CoA carboxylase and pyruvate carboxylase. Recombinant biotin protein ligase from S. aureus has been cloned, expressed and purified. Crystals were grown using the hanging-drop vapour-diffusion method using PEG 8000 as the precipitant at 295 K. X-ray diffraction data were collected to 2.3 A resolution from crystals using synchrotron X-ray radiation at 100 K. The diffraction was consistent with the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 93.665, c = 131.95.
AB - Biotin protein ligase from Staphylococcus aureus catalyses the biotinylation of acetyl-CoA carboxylase and pyruvate carboxylase. Recombinant biotin protein ligase from S. aureus has been cloned, expressed and purified. Crystals were grown using the hanging-drop vapour-diffusion method using PEG 8000 as the precipitant at 295 K. X-ray diffraction data were collected to 2.3 A resolution from crystals using synchrotron X-ray radiation at 100 K. The diffraction was consistent with the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 93.665, c = 131.95.
UR - http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2496860/pdf/f-64-00520.pdf
U2 - 10.1107/S1744309108012244
DO - 10.1107/S1744309108012244
M3 - Article
VL - 64
SP - 520
EP - 523
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
SN - 2053-230X
IS - Pt 6
ER -